P45118
Gene name |
aceF (HI_1232) |
Protein name |
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
Names |
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex, E2 |
Species |
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) |
KEGG Pathway |
hin:HI_1232 |
EC number |
2.3.1.12: Transferring groups other than amino-acyl groups |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for P45118
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P45118-F1 | Predicted | AlphaFoldDB |
No variants for P45118
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P45118 | |||||
No associated diseases with P45118
6 regional properties for P45118
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Biotin/lipoyl attachment | 2 - 75 | IPR000089-1 |
| domain | Biotin/lipoyl attachment | 108 - 181 | IPR000089-2 |
| domain | 2-oxoacid dehydrogenase acyltransferase, catalytic domain | 336 - 566 | IPR001078 |
| binding_site | 2-oxo acid dehydrogenase, lipoyl-binding site | 25 - 54 | IPR003016-1 |
| binding_site | 2-oxo acid dehydrogenase, lipoyl-binding site | 131 - 160 | IPR003016-2 |
| domain | Peripheral subunit-binding domain | 258 - 295 | IPR004167 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.3.1.12 | Transferring groups other than amino-acyl groups |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| pyruvate dehydrogenase complex | Complex that carries out the oxidative decarboxylation of pyruvate to form acetyl-CoA; comprises subunits possessing three catalytic activities: pyruvate dehydrogenase (E1), dihydrolipoamide S-acetyltransferase (E2), and dihydrolipoamide dehydrogenase (E3). |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| acetyltransferase activity | Catalysis of the transfer of an acetyl group to an acceptor molecule. |
| dihydrolipoyllysine-residue acetyltransferase activity | Catalysis of the reaction: acetyl-CoA + dihydrolipoamide = CoA + S-acetyldihydrolipoamide. |
| lipoic acid binding | Binding to lipoic acid, 1,2-dithiolane-3-pentanoic acid. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| acetyl-CoA biosynthetic process from pyruvate | The chemical reactions and pathways resulting in the formation of acetyl-CoA from pyruvate. |
| glycolytic process | The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSKQIQIPDI | GSDEVTVTEV | MVNVGDTISV | DQSIINVEGD | KASMEVPAPE | AGVVKEILVK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VGDKVSTGTP | MLVLEAAGAA | PAADEPTAPV | ADAPTAPVVA | TAPTASAIVE | VNVPDIGGDE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VNVTEIMVAV | GDTITEEQSL | ITVEGDKASM | EVPAPFGGVV | KEILVKSGDK | VSTGSLIMRF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EVLGAAPAES | ASAPASTSAP | QTAAPATTAQ | APQAAAPDTT | AQAPQAAAPD | TTAQAAQSNN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NVSGLSQEQV | EASTGYAHAT | PVIRRLAREF | GVNLDKVKGT | GRKGRIVKED | IEAYVKTAVK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AYESGATAQA | TGNGVANGAG | LGLLPWPKVD | FSKFGEIEEV | ELSRINKISG | ANLHRNWVII |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PHVTHFDKAD | ITDLEAFRKE | QNALREKQKL | GVKITPVVFI | MKAVAKALEA | YPRFNSSITE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| DAQRLILKKY | INIGVAVDTP | NGLVVPVFKN | VNKKGIIELS | RELMEVSKKA | REGKLTASDM |
| 490 | 500 | 510 | 520 | 530 | 540 |
| QGGCFTISSL | GGIGTTHFAP | IVNAPEVAIL | GVSKSSMEPV | WNGKEFAPRL | ILPMSLSFDH |
| 550 | 560 | ||||
| RVIDGADGAR | FISYLGSVLA | DLRRLVM |